Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases
- 6 January 1986
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 194 (2), 338-346
- https://doi.org/10.1016/0014-5793(86)80113-2
Abstract
There are 33 invariant amino acid positions out of 132 positions in 42 investigated sequences of ribonucleases from a number of mammalian species and a reptile (snapping turtle, Chelydra serpentina). These invariant residues are unequally distributed over 3 different parts of the molecule. The lobe of the S-protein part of the molecule, which lacks one disulfide bridge and has two shortened loops in turtle ribonuclease, has the lowest percentage of invariant residues, although the active-site residue His 119 is located in this part.Keywords
This publication has 20 references indexed in Scilit:
- Mammalian ribonucleasesFEBS Letters, 1985
- Rat pancreatic ribonuclease: agreement between the corrected amino acid sequence and the sequence derived from its messenger RNAFEBS Letters, 1983
- Ribonuclease-A: least-squares refinement of the structure at 1.45 Å resolutionActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1982
- The Amino‐Acid Sequence of Kangaroo Pancreatic RibonucleaseEuropean Journal of Biochemistry, 1978
- The molecular evolution of pancreatic ribonucleaseJournal of Molecular Evolution, 1977
- Invariant features of the structure of pancreatic ribonucleaseJournal of Molecular Biology, 1977
- Relationship between α-helical propensity and formation of the ribonuclease-S complexJournal of Molecular Biology, 1975
- Algorithms for prediction of α-helical and β-structural regions in globular proteinsJournal of Molecular Biology, 1974
- Prediction of protein conformationBiochemistry, 1974
- Biological Function of Pancreatic RibonucleaseNature, 1969